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Database: PDB
Entry: 5P21
LinkDB: 5P21
Original site: 5P21 
HEADER    ONCOGENE PROTEIN                        30-APR-90   5P21              
TITLE     REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION            
TITLE    2 OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS              
TITLE    3 FOR THE MECHANISM OF GTP HYDROLYSIS                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-H-RAS P21 PROTEIN;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    ONCOGENE PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.PAI,A.WITTINGHOFER,W.KABSCH                                       
REVDAT   5   24-FEB-09 5P21    1       VERSN                                    
REVDAT   4   01-APR-03 5P21    1       JRNL                                     
REVDAT   3   20-JUL-95 5P21    1       HET                                      
REVDAT   2   30-APR-94 5P21    1       FORMUL                                   
REVDAT   1   15-JAN-92 5P21    0                                                
JRNL        AUTH   E.F.PAI,U.KRENGEL,G.A.PETSKO,R.S.GOODY,W.KABSCH,             
JRNL        AUTH 2 A.WITTINGHOFER                                               
JRNL        TITL   REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE                
JRNL        TITL 2 CONFORMATION OF H-RAS P21 AT 1.35 A RESOLUTION:              
JRNL        TITL 3 IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS.            
JRNL        REF    EMBO J.                       V.   9  2351 1990              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   2196171                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.SCHLICHTING,S.C.ALMO,G.RAPP,K.WILSON,K.PETRATOS,           
REMARK   1  AUTH 2 A.LENTFER,A.WITTINGHOFER,W.KABSCH,E.F.PAI,                   
REMARK   1  AUTH 3 G.A.PETSKO,R.S.GOODY                                         
REMARK   1  TITL   TIME-RESOLVED X-RAY CRYSTALLOGRAPHIC STUDY OF THE            
REMARK   1  TITL 2 CONFORMATIONAL CHANGE IN HA-RAS P21 PROTEIN ON GTP           
REMARK   1  TITL 3 HYDROLYSIS                                                   
REMARK   1  REF    NATURE                        V. 345   309 1990              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.SCHERER,J.JOHN,R.LINKE,R.S.GOODY,A.WITTINGHOFER,           
REMARK   1  AUTH 2 E.F.PAI,K.C.HOLMES                                           
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF            
REMARK   1  TITL 2 THE HUMAN C-H-RAS-ONCOGENE PRODUCT P21 COMPLEXED             
REMARK   1  TITL 3 WITH GTP ANALOGUES                                           
REMARK   1  REF    J.MOL.BIOL.                   V. 206   257 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.F.PAI,W.KABSCH,U.KRENGEL,K.C.HOLMES,J.JOHN,                
REMARK   1  AUTH 2 A.WITTINGHOFER                                               
REMARK   1  TITL   STRUCTURE OF THE GUANINE-NUCLEOTIDE-BINDING DOMAIN           
REMARK   1  TITL 2 OF THE HA-RAS ONCOGENE PRODUCT P21 IN THE                    
REMARK   1  TITL 3 TRIPHOSPHATE CONFORMATION                                    
REMARK   1  REF    NATURE                        V. 341   209 1989              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   I.SCHLICHTING,G.RAPP,J.JOHN,A.WITTINGHOFER,E.F.PAI,          
REMARK   1  AUTH 2 R.S.GOODY                                                    
REMARK   1  TITL   BIOCHEMICAL AND CRYSTALLOGRAPHIC CHARACTERIZATION            
REMARK   1  TITL 2 OF A COMPLEX OF C-HA-RAS P21 AND CAGED GTP WITH              
REMARK   1  TITL 3 FLASH PHOTOLYSIS                                             
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  86  7687 1989              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 26806                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  RESIDUES 61 - 65 (GLN - GLU - GLU -      
REMARK   3  TYR - SER) ADOPT SEVERAL CONFORMATIONS IN THE CRYSTAL. THE          
REMARK   3  COORDINATES GIVEN APPROXIMATE ONE OF THESE.                         
REMARK   4                                                                      
REMARK   4 5P21 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.13333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.06667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       54.06667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.13333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A  97   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 123   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 135   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TYR A 157   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG A 164   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  33       75.86   -157.25                                   
REMARK 500    ILE A  36      -64.23   -100.39                                   
REMARK 500    GLU A  37      123.75   -171.30                                   
REMARK 500    SER A  65     -133.70     53.07                                   
REMARK 500    LYS A 117       33.80     71.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 224        DISTANCE =  9.45 ANGSTROMS                       
REMARK 525    HOH A 243        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A 249        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 252        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A 300        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH A 301        DISTANCE = 10.14 ANGSTROMS                       
REMARK 525    HOH A 303        DISTANCE = 10.91 ANGSTROMS                       
REMARK 525    HOH A 304        DISTANCE = 13.77 ANGSTROMS                       
REMARK 525    HOH A 306        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH A 307        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH A 311        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH A 321        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH A 331        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 366        DISTANCE =  8.86 ANGSTROMS                       
REMARK 525    HOH A 370        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A 379        DISTANCE = 11.13 ANGSTROMS                       
REMARK 525    HOH A 381        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 394        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 395        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH A 403        DISTANCE =  5.08 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 168  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP A 167   O2G                                                    
REMARK 620 2 GNP A 167   O2B  95.0                                              
REMARK 620 3 HOH A 173   O    87.6  91.7                                        
REMARK 620 4 SER A  17   OG  172.9  91.0  88.6                                  
REMARK 620 5 THR A  35   OG1  91.3 173.4  90.5  82.8                            
REMARK 620 6 HOH A 172   O    97.3  88.0 175.0  86.5  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 168                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 167                 
DBREF  5P21 A    1   166  UNP    P01112   RASH_HUMAN       1    166             
SEQRES   1 A  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY          
SEQRES   2 A  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 A  166  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 A  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 A  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER          
SEQRES   6 A  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 A  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 A  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 A  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 A  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA          
SEQRES  11 A  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU          
SEQRES  12 A  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE          
SEQRES  13 A  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                      
HET     MG  A 168       1                                                       
HET    GNP  A 167      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GNP    C10 H17 N6 O13 P3                                            
FORMUL   4  HOH   *211(H2 O)                                                    
HELIX    1  HA LYS A   16  GLN A   25  1                                  10    
HELIX    2  HB SER A   65  THR A   74  1RES 65-67 IN 3/10 CONF            10    
HELIX    3  HC THR A   87  VAL A  103  1BREAK AT ASP 92                   17    
HELIX    4  HD SER A  127  TYR A  137  1                                  11    
HELIX    5  HE VAL A  152  ARG A  164  1                                  13    
SHEET    1  S1 6 GLU A  37  ILE A  46  0                                        
SHEET    2  S1 6 GLU A  49  THR A  58 -1  O  LEU A  53   N  LYS A  42           
SHEET    3  S1 6 THR A   2  VAL A   9  1  N  LEU A   6   O  ASP A  54           
SHEET    4  S1 6 GLY A  77  ALA A  83  1  N  LEU A  79   O  VAL A   7           
SHEET    5  S1 6 MET A 111  ASN A 116  1  N  VAL A 114   O  CYS A  80           
SHEET    6  S1 6 TYR A 141  GLU A 143  1  N  ILE A 142   O  LEU A 113           
LINK        MG    MG A 168                 O2G GNP A 167     1555   1555  2.20  
LINK        MG    MG A 168                 O2B GNP A 167     1555   1555  2.22  
LINK        MG    MG A 168                 O   HOH A 173     1555   1555  2.23  
LINK        MG    MG A 168                 OG  SER A  17     1555   1555  2.26  
LINK        MG    MG A 168                 OG1 THR A  35     1555   1555  2.26  
LINK        MG    MG A 168                 O   HOH A 172     1555   1555  2.30  
SITE     1 AC1  5 SER A  17  THR A  35  GNP A 167  HOH A 172                    
SITE     2 AC1  5 HOH A 173                                                     
SITE     1 AC2 28 GLY A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 28 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC2 28 VAL A  29  ASP A  30  TYR A  32  PRO A  34                    
SITE     4 AC2 28 THR A  35  GLY A  60  ASN A 116  LYS A 117                    
SITE     5 AC2 28 ASP A 119  SER A 145  ALA A 146  LYS A 147                    
SITE     6 AC2 28  MG A 168  HOH A 170  HOH A 172  HOH A 173                    
SITE     7 AC2 28 HOH A 175  HOH A 187  HOH A 281  HOH A 366                    
CRYST1   40.300   40.300  162.200  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024814  0.014326  0.000000        0.00000                         
SCALE2      0.000000  0.028653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006165        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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